The periplasmic component of the DctPQM TRAP-transporter is part of the DctS/DctR sensory pathway in Rhodobacter sphaeroides

Rhodobacter sphaeroides can use C4-dicarboxylic acids to grow heterotrophically or photoheterotropically, and it was previously demonstrated in Rhodobacter capsulatus that the DctPQM transporter system is essential to support growth using these organic acids under heterotrophic but not under photoheterotrophic conditions. In this work we show that in R. sphaeroides this transporter system is essential for photoheterotrophic and heterotrophic growth, when C4-dicarboxylic acids are used as a carbon source. We also found that over-expression of dctPQM is detrimental for photoheterotrophic growth in the presence of succinic acid in the culture medium. In agreement with this, we observed a reduction of the dctPQM promoter activity in cells growing under these conditions, indicating that the amount of DctPQM needs to be reduced under photoheterotrophic growth. It has been reported that the two-component system DctS and DctR activates the expression of dctPQM. Our results demonstrate that in the absence of DctR, dctPQM is still expressed albeit at a low level. In this work, we have found that the periplasmic component of the transporter system, DctP, has a role in both transport and in signalling the DctS/DctR two-component system.

Photoheterotrophic growth of unicellular cyanobacterium Synechocystis sp. PCC 6803 gtr− dependent on fructose

Although cyanobacteria have specialized for a photolithoautotrophic mode of life during evolution many cyanobacterial strains have been identified as being capable of photoheterotrophy or even chemoheterotrophy. The mutant strain of Synechocystis sp. PCC 6803, which lacks the gtr gene coding for the strain’s glucose/fructose permease, has been believed to be a strict photolithoautotroph in the past as it has lost the wild type’s facility to use external glucose for both photoheterotrophy and light-induced chemoheterotrophy. However, recent experiments revealed the strain’s capacity to use fructose for mixotrophic and photoheterotrophic growth, a sugar which is toxic for the wild type. Both the growth rate and the amount of fructose incorporated into the cells increased along with the fructose concentrations in the surrounding medium. Furthermore an increase of the total carbon mass of the cells within a liquid culture over a period of photoheterotrophic growth could be demonstrated. Contrary to the wild type, glucose could not be used for photoheterotrophic growth, and chemoheterotrophic growth failed with fructose as well as with glucose. Graphic abstract

Different Functions of Phylogenetically Distinct Bacterial Complex I Isozymes

ABSTRACTNADH:quinone oxidoreductase (complex I) is a bioenergetic enzyme that transfers electrons from NADH to quinone, conserving the energy of this reaction by contributing to the proton motive force. While the importance of NADH oxidation to mitochondrial aerobic respiration is well documented, the contribution of complex I to bacterial electron transport chains has been tested in only a few species. Here, we analyze the function of two phylogenetically distinct complex I isozymes inRhodobacter sphaeroides, an alphaproteobacterium that contains well-characterized electron transport chains. We found thatR. sphaeroidescomplex I activity is important for aerobic respiration and required for anaerobic dimethyl sulfoxide (DMSO) respiration (in the absence of light), photoautotrophic growth, and photoheterotrophic growth (in the absence of an external electron acceptor). Our data also provide insight into the functions of the phylogenetically distinctR. sphaeroidescomplex I enzymes (complex IAand complex IE) in maintaining a cellular redox state during photoheterotrophic growth. We propose that the function of each isozyme during photoheterotrophic growth is either NADH synthesis (complex IA) or NADH oxidation (complex IE). The canonical alphaproteobacterial complex I isozyme (complex IA) was also shown to be important for routing electrons to nitrogenase-mediated H2production, while the horizontally acquired enzyme (complex IE) was dispensable in this process. Unlike the singular role of complex I in mitochondria, we predict that the phylogenetically distinct complex I enzymes found across bacterial species have evolved to enhance the functions of their respective electron transport chains.IMPORTANCECells use a proton motive force (PMF), NADH, and ATP to support numerous processes. In mitochondria, complex I uses NADH oxidation to generate a PMF, which can drive ATP synthesis. This study analyzed the function of complex I in bacteria, which contain more-diverse and more-flexible electron transport chains than mitochondria. We tested complex I function inRhodobacter sphaeroides, a bacterium predicted to encode two phylogenetically distinct complex I isozymes.R. sphaeroidescells lacking both isozymes had growth defects during all tested modes of growth, illustrating the important function of this enzyme under diverse conditions. We conclude that the two isozymes are not functionally redundant and predict that phylogenetically distinct complex I enzymes have evolved to support the diverse lifestyles of bacteria.